Activity of fructanase in batch cultures of oral streptococci

Carbohydr Res. 1983 Feb 16;113(1):101-12. doi: 10.1016/0008-6215(83)88222-6.


Several strains of oral streptococci produced fructanase when grown in the absence of D-fructan in a complex medium supplemented with D-glucose. The major part of the activity was extracellular, and only 1-5% was associated with the cells. Release of fructanase began early in the exponential phase and the enzyme was stable in the stationary phase for several h if the pH did not fall below 6. Among the strains of Streptococcus mutans, serotypes a, d, and g released the highest amount of fructanase, and the low level of enzyme produced by strains of serotype c was increased when D-fructose replaced D-glucose as carbon source for growth. Fructanase of S. mutans readily hydrolysed (2 leads to 6)-beta-D-fructans, but (2 leads to 1)-beta-D-fructans and inulin were more resistant. Adsorption of fructanase to (2 leads to 6)-beta-D-fructan, or inhibition with Tris buffer, provided effective means of eliminating fructanase activity from culture filtrates. This procedure should permit a more accurate determination of fructosyltransferase activity of S. mutans strains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Child
  • Dental Plaque / microbiology*
  • Glycoside Hydrolases / metabolism*
  • Humans
  • Kinetics
  • Species Specificity
  • Streptococcus / enzymology
  • Streptococcus mutans / enzymology*
  • Streptococcus mutans / growth & development


  • Bacterial Proteins
  • Glycoside Hydrolases
  • levanase